title: The three-dimensional structure of the seed storage protein phaseolin at 3 A resolution.
abstract: The polypeptides of the trimeric seed storage protein phaseolin comprise two structurally similar units each made up of a beta-barrel and an alpha-helical domain. The beta-barrel has the 'jelly-roll' folding topology of the viral coat proteins and the alpha-helical domain shows structural similarity to the helix-turn-helix motif found in certain DNA-binding proteins.
authors.affiliation: CSIRO Division of Biotechnology, Parkville, Victoria, Australia.
authors.forename: M C
authors.initials: MC
authors.lastname: Lawrence
authors.forename: E
authors.initials: E
authors.lastname: Suzuki
authors.forename: J N
authors.initials: JN
authors.lastname: Varghese
authors.forename: P C
authors.initials: PC
authors.lastname: Davis
authors.forename: A
authors.initials: A
authors.lastname: Van Donkelaar
authors.forename: P A
authors.initials: PA
authors.lastname: Tulloch
authors.forename: P M
authors.initials: PM
authors.lastname: Colman
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D003460:Crystallization; D006031:Glycosylation; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010940:Plant Proteins; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D046911:Macromolecular Substances; D010940:Plant Proteins; C048826:phaseolin protein, Phaseolus vulgaris